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Renal Actions of Vasopressin

Mark A. Knepper, Heinz Valtin, Jeff M. Sands

10.1002/cphy.cp070313

Source: Supplement 22: Handbook of Physiology, The Endocrine System, Endocrine Regulation of Water and Electrolyte Balance

Originally published: 2000

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Vasopressin and the Urinary Concentrating and Diluting Mechanism
1.1 General Features of the Urinary Concentration and Dilution Process
1.2 Mechanism of Tubule Fluid Dilution
1.3 Mechanism of Tubule Fluid Concentration
1.4 Countercurrent Multiplication
1.5 Role of Vasopressin in Urinary Concentration and Dilution
2 Vasopressin Receptors
2.1 V1a and V1b Receptor Subtypes
2.2 V2 Receptors
2.3 Renal Localization
3 Regulation of Aquaporin Water Channels by Vasopressin
3.1 Aquaporin Structure
3.2 Localization of Aquaporins in the Kidney
3.3 Short‐ and Long‐Term Regulation of Water Permeability in the Collecting Duct
3.4 Short‐Term Regulation of Aquaporin‐2 by Vasopressin‐Induced Trafficking
3.5 Long‐Term Regulation of Water Transport Through Regulation of Aquaporin Protein Abundance
3.6 Role of Vasopressin in Pathophysiological Stales Associated with Abnormalities of Water Balance
4 The Vasopressin‐Regulated Urea Transporter
4.1 Physiological Evidence for a Vasopressin‐Regulated Urea Transporter
4.2 Molecular Cloning of Renal Urea Transporters
4.3 Short‐Term Regulation
4.4 Long‐Term Regulation
5 Regulation of Loop of Henle Function by Vasopressin
5.1 Thick Ascending Limb
5.2 Thin Ascending Limb
6 Regulation of Renal Hemodynamics by Vasopressin
6.1 Medullary Blood Flow
6.2 Glomerular Function
Figure 1. Figure 1.

Steady‐state renal response to varying rates of vasopressin infusion in conscious rats. A water load (4% of body weight) was maintained throughout the experiments to suppress endogenous vasopressin secretion. A: Water excretion and osmolar clearance (Cosm). Although water excretion was markedly reduced at higher vasopressin infusion rates, osmolar clearance changed very little. B: Urinary osmolality. [Data plotted from Atherton et al. 12.]
Figure 2. Figure 2.

Mammalian renal structure. Major regions of the kidney are labeled at left. Configurations of a long‐looped (left) and a short‐looped (right) nephron are depicted. The major portions of the nephron are proximal tubules (hatched), thin limbs of Henle's loops (single line), thick ascending limbs of Henle's loops (solid), distal convoluted tubules (stippled), and the collecting duct system (open). OS, outer stripe; IS, inner stripe.
Figure 3. Figure 3.

Osmolality measurements at different points along the renal tubule at high and low circulating vasopressin levels. Data are typical osmolalities (in milliosmoles per kilogram H2O) found in various renal tubular sites by micropuncture in anesthetized rodents 92, 121, 277. Fluid in the proximal tubule is always virtually isosmotic with plasma (290 mOsm/kg H2O). Fluid emerging from the loop of Henle (entering early distal tubule) is always hypotonic. Osmolality in the late distal tubule increases to the plasma level only when circulating vasopressin is high. Final urine is hypertonic when circulating vasopressin is high, hypotonic when vasopressin is low. A high osmolality is always maintained in the loop of Henle, though the value is somewhat attenuated at low vasopressin levels. With high circulating vasopressin levels, osmolalities in all inner medullary structures are nearly equal. AVP, arginine vasopressin.
Figure 4. Figure 4.

Composition of rat renal medullary tissue and urine with high (left) and low (right) circulating vasopressin levels. IS, inner stripe of outer medulla; OS, outer stripe of outer medulla. [Data from Hai and Thomas 97.]
Figure 5. Figure 5.

Membrane‐spanning architecture of V2 vasopressin receptor. The V2 receptor is a single polypeptide chain that spans the plasma membrane seven times, as is characteristic among the super‐family of G protein–coupled receptors. The amino terminus is extracellular, while the carboxy terminus is intracellular. A putative glycosylation site is located in the extracellular amino‐terminal region (arrowhead). The site of ligand‐induced posttranslational cleavage by a membrane metalloproteinase 146 is indicated by arrows. There is a disulfide bridge between cysteine residues in the first and second extracellular loops. The carboxy terminus is palmitoylated, which provides an additional site of attachment to the plasma membrane. [From Fahrenholz et al. 68 with permission.]
Figure 6. Figure 6.

Localization of vasopressin receptor mRNA in rat kidney by in situ hybridization. White areas indicate sites of hybridization with antisense probes. Left panel: V1a receptor. High‐resolution studies showed labeling of inner medullary structures between the collecting ducts but no labeling of the collecting ducts themselves. Right panel: V2 receptor. High‐resolution studies showed heavy labeling of all collecting duct segments and moderate labeling of medullary thick ascending limbs. Controls with sense probes gave no labeling (not shown). [From Ostrowski et al. 206 with permission.]
Figure 7. Figure 7.

Membrane‐spanning architecture of aquaporins. Each molecule spans the plasma membrane six times, with the amino and carboxy termini in the intracellular milieu. Loops are labeled A through E according to the terminology of Agre and colleagues 125. Aquaporins contain a characteristic asparagine‐proline‐alanine (NPA) sequence in the B and E loops, which is postulated to play a role in forming the water pore 125. The greatest variability among the four renal aquaporins is in the COOH termini. This variability allowed unique peptides to be synthesized for each aquaporin, facilitating the preparation of specific polyclonal antibodies to each.
Figure 8. Figure 8.

Immunogold labeling with anti‐aquaporin‐2 antibody in principal cells from isolated perfused inner medullary collecting ducts. The three panels show typical sections from tubules fixed before (A), during (B), and after (C) exposure to arginine vasopressin (AVP). Small arrows point to selected sites of apical plasma membrane labeling, while arrowheads indicate sites of vesicular labeling. Note shift of labeling from intracellular vesicles to plasma membrane in response to arginine vasopressin exposure of perfused collecting duct. Statistical analysis of labeling distribution in 30 different perfused segments showed a highly significant shift from vesicles to plasma membrane in response to arginine vasopressin. MVB, multivesicular body. [From Nielsen et al. 192 with permission.]
Figure 9. Figure 9.

Diagram of collecting duct principal cell indicating distribution of aquaporins and mechanism by which water permeability of the apical plasma membrane increases in response to a vasopressin‐induced increase in intracellular cAMP. Aquaporin‐2 is present in the apical plasma membrane and in intracellular vesicles and shuttles between these two compartments depending on the vasopressin‐induced level of intracellular cAMP. Aquaporin‐3 and aquaporin‐4 are present in the basolateral plasma membrane and are thought to be responsible for the constitutively high water permeability of the basolateral barrier.
Figure 10. Figure 10.

Effect of restriction of water intake in rats (Thirsted) on osmotic water permeability (A) and urea permeability (B) of isolated perfused inner medullary collecting ducts. Measurements were made in the absence of in vitro vasopressin after a long equilibration period. Thirsting resulted in a conditioned increase in water permeability but not urea permeability. [Bar graphs were drawn using data from Lankford et al. 159.]
Figure 11. Figure 11.

Transepithelial urea permeability in isolated collecting ducts and papillary surface epithelium measured in the presence and absence of arginine vasopressin (AVP). Vasopressin increases urea permeability only in the terminal portion of the inner medullary collecting duct. CCD, cortical collecting duct; OMCD, outer medullary collecting duct; IMCD, inner medullary collecting duct; PSE, papillary surface epithelium. [Data are plotted from 223, 225.]
Figure 12. Figure 12.

Comparison of epithelial urea permeability in various renal tubule segments (solid bars) with predicted values assuming urea is transported only by lipid phase diffusion (hatched bars). Predicted values include an estimate of apical and basolateral membrane amplification due to apical projections and basolateral infoldings, assuming that urea permeabilities of apical and basolateral membranes are the same as in artificial phospholipid bilayers (4 × 10−6 cm/sec) 82. PCT, proximal convoluted tubule; PST, proximal straight tubule; tAL, thin ascending limb; mTAL, medullary thick ascending limb; cTAL, cortical thick ascending limb; CCD, cortical collecting duct; OMCD, outer medullary collecting duct; IMCD, inner medullary collecting duct; PSE, papillary surface epithelium. [Data of Sands et al. 225].
Figure 13. Figure 13.

Renal urea transporter gene splice variants. A: UTA‐1 cDNA codes for a 929 amino acid protein. This isoform is expressed in the IMCD and is the vasopressin‐regulated urea transporter. B: UTA‐2 cDNA codes for a 397 amino acid protein that is identical to the terminal 397 amino acid sequence of the UTA‐1 protein. UTA‐2 is expressed in the cells of the descending limb of Henle's loop. H1–H4 designate 134 amino acid hydrophobic regions that presumably span the plasma membrane one or more times.
Figure 14. Figure 14.

Cell model of thick ascending limb epithelial transporters.


Figure 1.

Steady‐state renal response to varying rates of vasopressin infusion in conscious rats. A water load (4% of body weight) was maintained throughout the experiments to suppress endogenous vasopressin secretion. A: Water excretion and osmolar clearance (Cosm). Although water excretion was markedly reduced at higher vasopressin infusion rates, osmolar clearance changed very little. B: Urinary osmolality. [Data plotted from Atherton et al. 12.]



Figure 2.

Mammalian renal structure. Major regions of the kidney are labeled at left. Configurations of a long‐looped (left) and a short‐looped (right) nephron are depicted. The major portions of the nephron are proximal tubules (hatched), thin limbs of Henle's loops (single line), thick ascending limbs of Henle's loops (solid), distal convoluted tubules (stippled), and the collecting duct system (open). OS, outer stripe; IS, inner stripe.



Figure 3.

Osmolality measurements at different points along the renal tubule at high and low circulating vasopressin levels. Data are typical osmolalities (in milliosmoles per kilogram H2O) found in various renal tubular sites by micropuncture in anesthetized rodents 92, 121, 277. Fluid in the proximal tubule is always virtually isosmotic with plasma (290 mOsm/kg H2O). Fluid emerging from the loop of Henle (entering early distal tubule) is always hypotonic. Osmolality in the late distal tubule increases to the plasma level only when circulating vasopressin is high. Final urine is hypertonic when circulating vasopressin is high, hypotonic when vasopressin is low. A high osmolality is always maintained in the loop of Henle, though the value is somewhat attenuated at low vasopressin levels. With high circulating vasopressin levels, osmolalities in all inner medullary structures are nearly equal. AVP, arginine vasopressin.



Figure 4.

Composition of rat renal medullary tissue and urine with high (left) and low (right) circulating vasopressin levels. IS, inner stripe of outer medulla; OS, outer stripe of outer medulla. [Data from Hai and Thomas 97.]



Figure 5.

Membrane‐spanning architecture of V2 vasopressin receptor. The V2 receptor is a single polypeptide chain that spans the plasma membrane seven times, as is characteristic among the super‐family of G protein–coupled receptors. The amino terminus is extracellular, while the carboxy terminus is intracellular. A putative glycosylation site is located in the extracellular amino‐terminal region (arrowhead). The site of ligand‐induced posttranslational cleavage by a membrane metalloproteinase 146 is indicated by arrows. There is a disulfide bridge between cysteine residues in the first and second extracellular loops. The carboxy terminus is palmitoylated, which provides an additional site of attachment to the plasma membrane. [From Fahrenholz et al. 68 with permission.]



Figure 6.

Localization of vasopressin receptor mRNA in rat kidney by in situ hybridization. White areas indicate sites of hybridization with antisense probes. Left panel: V1a receptor. High‐resolution studies showed labeling of inner medullary structures between the collecting ducts but no labeling of the collecting ducts themselves. Right panel: V2 receptor. High‐resolution studies showed heavy labeling of all collecting duct segments and moderate labeling of medullary thick ascending limbs. Controls with sense probes gave no labeling (not shown). [From Ostrowski et al. 206 with permission.]



Figure 7.

Membrane‐spanning architecture of aquaporins. Each molecule spans the plasma membrane six times, with the amino and carboxy termini in the intracellular milieu. Loops are labeled A through E according to the terminology of Agre and colleagues 125. Aquaporins contain a characteristic asparagine‐proline‐alanine (NPA) sequence in the B and E loops, which is postulated to play a role in forming the water pore 125. The greatest variability among the four renal aquaporins is in the COOH termini. This variability allowed unique peptides to be synthesized for each aquaporin, facilitating the preparation of specific polyclonal antibodies to each.



Figure 8.

Immunogold labeling with anti‐aquaporin‐2 antibody in principal cells from isolated perfused inner medullary collecting ducts. The three panels show typical sections from tubules fixed before (A), during (B), and after (C) exposure to arginine vasopressin (AVP). Small arrows point to selected sites of apical plasma membrane labeling, while arrowheads indicate sites of vesicular labeling. Note shift of labeling from intracellular vesicles to plasma membrane in response to arginine vasopressin exposure of perfused collecting duct. Statistical analysis of labeling distribution in 30 different perfused segments showed a highly significant shift from vesicles to plasma membrane in response to arginine vasopressin. MVB, multivesicular body. [From Nielsen et al. 192 with permission.]



Figure 9.

Diagram of collecting duct principal cell indicating distribution of aquaporins and mechanism by which water permeability of the apical plasma membrane increases in response to a vasopressin‐induced increase in intracellular cAMP. Aquaporin‐2 is present in the apical plasma membrane and in intracellular vesicles and shuttles between these two compartments depending on the vasopressin‐induced level of intracellular cAMP. Aquaporin‐3 and aquaporin‐4 are present in the basolateral plasma membrane and are thought to be responsible for the constitutively high water permeability of the basolateral barrier.



Figure 10.

Effect of restriction of water intake in rats (Thirsted) on osmotic water permeability (A) and urea permeability (B) of isolated perfused inner medullary collecting ducts. Measurements were made in the absence of in vitro vasopressin after a long equilibration period. Thirsting resulted in a conditioned increase in water permeability but not urea permeability. [Bar graphs were drawn using data from Lankford et al. 159.]



Figure 11.

Transepithelial urea permeability in isolated collecting ducts and papillary surface epithelium measured in the presence and absence of arginine vasopressin (AVP). Vasopressin increases urea permeability only in the terminal portion of the inner medullary collecting duct. CCD, cortical collecting duct; OMCD, outer medullary collecting duct; IMCD, inner medullary collecting duct; PSE, papillary surface epithelium. [Data are plotted from 223, 225.]



Figure 12.

Comparison of epithelial urea permeability in various renal tubule segments (solid bars) with predicted values assuming urea is transported only by lipid phase diffusion (hatched bars). Predicted values include an estimate of apical and basolateral membrane amplification due to apical projections and basolateral infoldings, assuming that urea permeabilities of apical and basolateral membranes are the same as in artificial phospholipid bilayers (4 × 10−6 cm/sec) 82. PCT, proximal convoluted tubule; PST, proximal straight tubule; tAL, thin ascending limb; mTAL, medullary thick ascending limb; cTAL, cortical thick ascending limb; CCD, cortical collecting duct; OMCD, outer medullary collecting duct; IMCD, inner medullary collecting duct; PSE, papillary surface epithelium. [Data of Sands et al. 225].



Figure 13.

Renal urea transporter gene splice variants. A: UTA‐1 cDNA codes for a 929 amino acid protein. This isoform is expressed in the IMCD and is the vasopressin‐regulated urea transporter. B: UTA‐2 cDNA codes for a 397 amino acid protein that is identical to the terminal 397 amino acid sequence of the UTA‐1 protein. UTA‐2 is expressed in the cells of the descending limb of Henle's loop. H1–H4 designate 134 amino acid hydrophobic regions that presumably span the plasma membrane one or more times.



Figure 14.

Cell model of thick ascending limb epithelial transporters.

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Article Title: Renal Actions of Vasopressin
 

How to Cite

Mark A. Knepper, Heinz Valtin, Jeff M. Sands. Renal Actions of Vasopressin. Compr Physiol 2011, Supplement 22: Handbook of Physiology, The Endocrine System, Endocrine Regulation of Water and Electrolyte Balance: 496-529. First published in print 2000. doi: 10.1002/cphy.cp070313